Investigating the role of large-scale domain dynamics in protein-protein interactions

Elise Delaforge; Sigrid Milles; Jie Rong Huang; Denis Bouvier; Malene Ringkjøbing Jensen; Michael Sattler; Darren J. Hart; Martin Blackledge

doi:10.3389/fmolb.2016.00054

Investigating the role of large-scale domain dynamics in protein-protein interactions

Elise Delaforge, Sigrid Milles, Jie Rong Huang, Denis Bouvier, Malene Ringkjøbing Jensen, Michael Sattler, Darren J. Hart, Martin Blackledge^*

^*Corresponding author for this work

Institute of Biochemistry and Molecular Biology

Research output: Contribution to journal › Short survey › peer-review

18 Scopus citations

Abstract

Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.

Original language	English
Article number	54
Journal	Frontiers in Molecular Biosciences
Volume	3
Issue number	SEP
DOIs	https://doi.org/10.3389/fmolb.2016.00054
State	Published - 13 Sep 2016

Keywords

Chemical exchange saturation transfer (CEST)
Conformational dynamics
Free-energy landscape
Multi-domain proteins
Nuclear magnetic resonance (NMR)
Single molecule Förster resonance energy transfer (FRET)
Small angle scattering

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10.3389/fmolb.2016.00054

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title = "Investigating the role of large-scale domain dynamics in protein-protein interactions",

abstract = "Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.",

keywords = "Chemical exchange saturation transfer (CEST), Conformational dynamics, Free-energy landscape, Multi-domain proteins, Nuclear magnetic resonance (NMR), Single molecule F{\"o}rster resonance energy transfer (FRET), Small angle scattering",

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note = "Publisher Copyright: {\textcopyright} 2016 Delaforge, Milles, Huang, Bouvier, Jensen, Sattler, Hart and Blackledge.",

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doi = "10.3389/fmolb.2016.00054",

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T1 - Investigating the role of large-scale domain dynamics in protein-protein interactions

AU - Delaforge, Elise

AU - Milles, Sigrid

AU - Huang, Jie Rong

AU - Bouvier, Denis

AU - Jensen, Malene Ringkjøbing

AU - Sattler, Michael

AU - Hart, Darren J.

AU - Blackledge, Martin

PY - 2016/9/13

Y1 - 2016/9/13

N2 - Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.

AB - Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a considerable challenge. Here we describe the difficulties associated with mapping the large-scale domain dynamics and describe two recent examples where solution state methods, in particular NMR spectroscopy, are used to investigate conformational exchange on very different timescales.

KW - Chemical exchange saturation transfer (CEST)

KW - Conformational dynamics

KW - Free-energy landscape

KW - Multi-domain proteins

KW - Nuclear magnetic resonance (NMR)

KW - Single molecule Förster resonance energy transfer (FRET)

KW - Small angle scattering

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DO - 10.3389/fmolb.2016.00054

M3 - Short survey

AN - SCOPUS:85020742366

SN - 2296-889X

VL - 3

JO - Frontiers in Molecular Biosciences

JF - Frontiers in Molecular Biosciences

IS - SEP

M1 - 54

ER -

Investigating the role of large-scale domain dynamics in protein-protein interactions

Abstract

Keywords

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